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Utilising crosslinking MS to explore protein structure and interactions

ABSTRACT: In this study, we performed proteome-wide crosslinking mass spectrometry (XLMS) on human HEK293 intact organelles and examined the combined utility of these crosslinks with AlphaFold.

INSTRUMENT(S): Orbitrap Fusion ETD, Q Exactive HF-X

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Jason Low

LAB HEAD: Jason Low

PROVIDER: PXD035844 | Pride | 2023-04-24

REPOSITORIES: Pride

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			Action	DRS
	20181108_Fusion_JL_exp1_CPF1.raw	Raw
	20181108_Fusion_JL_exp1_CPF10.raw	Raw
	20181108_Fusion_JL_exp1_CPF11.raw	Raw
	20181108_Fusion_JL_exp1_CPF12.raw	Raw
	20181108_Fusion_JL_exp1_CPF13.raw	Raw

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Publications

Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein-protein interactions in the human cell.

Bartolec Tara K TK Vázquez-Campos Xabier X Norman Alexander A Luong Clement C Johnson Marcus M Payne Richard J RJ Wilkins Marc R MR Mackay Joel P JP Low Jason K K JKK

Proceedings of the National Academy of Sciences of the United States of America 20230418 17

Significant recent advances in structural biology, particularly in the field of cryoelectron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory to these approaches because of their low abundance, low stability, or-in the case of complexes-simply not having yet been analyzed. Here, we demonstrate the power of using cross-linking mass spectrometry (XL-MS) for the high-throughput experimental ass ...[more]

PMID: 37071682

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